5XY9: MST4 and 14-3-3 complex

Structure of the MST4 and 14-3-3 complex. Determined by X-ray diffraction at 2.3 Å resolution. Released 11 Jul 2018.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,859
Mol. weight: 64.41 kDa
Ligands: PE4
Released: 11 Jul 2018

Explore 5XY9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5XY9 contains 30 α-helices and 0 β-strands across 3 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 15 helices, 0 β-strands

Element	Residues	Length
α-helix	2-15	14
α-helix	19-31	13
α-helix	35-36	2
α-helix	38-68	31
α-helix	73-100	28
α-helix	101-105	5
α-helix	106-108	3
α-helix	112-130	19
α-helix	136-148	13
α-helix	152-159	8
α-helix	165-176	12
α-helix	177-181	5
α-helix	185-200	16
α-helix	203-205	3
α-helix	211-231	21

Chain B: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	3-15	13
α-helix	19-31	13
α-helix	35-36	2
α-helix	38-67	30
α-helix	73-100	28
α-helix	101-105	5
α-helix	106-108	3
α-helix	112-132	21
α-helix	136-159	24
α-helix	165-176	12
α-helix	177-181	5
α-helix	185-200	16
α-helix	203-205	3
α-helix	211-229	19

Chain C: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	317-319	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
14-3-3 protein zeta/delta	A, B	protein	267	Homo sapiens	P63104 (AlphaFold model)
Peptide from Serine/threonine-protein kinase 26	C, D	protein	12	Homo sapiens	Q9P289 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5XY9_1 14-3-3 protein zeta/delta (chains A, B)
MSYYHHHHHHLESTSLYKKAGLMDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSN
EERNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVL
SLLEKFLIPNASQAESKVFYLKMKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKK
EMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIM
QLLRDNLTLWTSDTQGDEAEAGEGGEN

Sequence of entity 2 (C, D), FASTA

>5XY9_2 Peptide from Serine/threonine-protein kinase 26 (chains C, D)
TSRENNTHPEWS

Ligands and cofactors

ID	Name	Formula	Copies
PE4	2-{2-[2-(2-{2-[2-(2-ethoxy-ethoxy)-ethoxy]-ethoxy}-ethoxy)-ethoxy]-ethoxy}-etha…	C16 H34 O8	1

Water and common crystallization additives (GOL) are not listed.

Primary citation

Structure of the MST4 and 14-3-3 complex. Shi, Z., Zhou, Z. To be published.

Other PDB entries of the same protein (UniProt P63104 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2O02 1.5 Å, Phosphorylation independent interactions between 14-3-3 and Exoenzyme S: from structure…
6F09 1.59 Å, Binary complex of 14-3-3 zeta with ubiquitin specific protease 8 (USP8) pSer718 peptide
7ZIT 1.79 Å, 14-3-3 in complex with SARS-COV2 N phospho-peptide
9UJ2 1.8 Å, 14-3-3 zeta chimera with the S202R peptide of SARS-CoV-2 N (residues 200-213)
6ZFG 1.85 Å, 14-3-3 zeta chimera with 18E6 and fusicoccin
6F08 1.9 Å, 14-3-3 zeta in complex with the human Son of sevenless homolog 1 (SOS1)
6ZFD 1.9 Å, 14-3-3 zeta bound to the phosphorylated 18E6 C-terminus
4FJ3 1.95 Å, 14-3-3 isoform zeta in complex with a diphoyphorylated C-RAF peptide
5EXA 1.95 Å, Small-molecule stabilization of the 14-3-3/Gab2 PPI interface
8P1H 1.95 Å, Crystal structure of the chimera of human 14-3-3 zeta and phosphorylated cytoplasmic…
8A9G 1.96 Å, Binary complex of 14-3-3 zeta Glucocorticoid Receptor (GR) pT524 peptide stabilised by…
1QJA 2.0 Å, 14-3-3 zeta/phosphopeptide complex (mode 2)

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